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Conserved domains on  [gi|1173344|sp|P06105|]
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RecName: Full=Protein SCP160; AltName: Full=Protein HX

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 172-257 1.40e-33

first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the first one.


:

Pssm-ID: 411874 [Multi-domain]  Cd Length: 86  Bit Score: 124.44  E-value: 1.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   172 KKLTKPINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMDDTTSNVSLFGDFESVNLAKAKILA 251
Cdd:cd22446    1 KELSPKVTITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNEEGNYDEDDDDETVEISIEGDAEGVELAKKEIEA 80


                 ....*.
gi 1173344   252 IVKEET 257
Cdd:cd22446   81 IVKERT 86
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 632-707 4.77e-30

second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the second one.


:

Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 114.05  E-value: 4.77e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   632 SSKSKMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNAS----KDKTVEVTLTGLEYNLTHAKKYLAAEAK 707
Cdd:cd22447    1 SPKQNLTVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPadedDDTMVEVTITGDEFNVQHAKQRIEEIIS 80
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 711-777 3.00e-29

third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the third one.


:

Pssm-ID: 411876  Cd Length: 81  Bit Score: 111.85  E-value: 3.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   711 DIITKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDN--------------EIVTIRGPSRGVNKAHEELKALLD 776
Cdd:cd22448    1 DETTLILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPRENsssndtetkkpqapDEVTIRGGKKGVAEAKQELLELLE 80


                 .
gi 1173344   777 F 777
Cdd:cd22448   81 Y 81
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 940-1008 5.21e-27

sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the sixth one.


:

Pssm-ID: 411879 [Multi-domain]  Cd Length: 69  Bit Score: 104.84  E-value: 5.21e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   940 VTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKILNEIIRE 1008
Cdd:cd22451    1 ASIDIDIPKEYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGKIRITGARDGVEAATAKILNISDEE 69
KH-I_ScSCP160_rpt5 cd22450
fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 859-935 6.72e-27

fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fifth one.


:

Pssm-ID: 411878  Cd Length: 80  Bit Score: 105.05  E-value: 6.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   859 SDFVTEVLKIDHKYHKSIVGSGGHILREIISKAGG---EEIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEINKIVKD 935
Cdd:cd22450    1 EDEVTRTIKVDRKYHRTIIGPGGSTLRELISKAGGptdRQEQARLVRFPNQNSESDEVVIRGPKKIVEKIIAEIEKIVEE 80
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1152-1218 1.37e-22

seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the seventh one.


:

Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 92.00  E-value: 1.37e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344  1152 TYAGYVWGADtRRFNMIVGPGGSNIKKIREAADVIINVPRKsDKVNDVVYIRGTKAGVEKAGEMVLK 1218
Cdd:cd22452    1 DFRGWIKVSP-RYFGRIIGPGGSNINQIREKSGCFINVPKK-NKESDVITLRGTKEGVEKAEEMIKK 65
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 780-857 2.75e-21

fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


:

Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 88.48  E-value: 2.75e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344   780 ENGHKMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKstdpkaqeTGEVELEITGSRQNIKDAAKRVESIVAE 857
Cdd:cd22449    1 ENGYTVKFDVPAKYVPHIIGKKGANINKLREEYGVKIDFEDK--------TGEGNVEIKGSKKNVEEAKKRILSQIDE 70
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 502-606 2.15e-03

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member PRK15460:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 478  Bit Score: 42.27  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344    502 ESSVAFVQFGDYYPNDNSILLVA---LTEDEDFKPSI-EEIQASLNKANESLNSLRTKQNNM-----ETKTYEFSEEVQD 572
Cdd:PRK15460  188 ETAQAYVASGEYYWNSGMFLFRAgryLEELKKYRPDIlDACEKAMSAVDPDLDFIRVDEEAFlacpeESVDYAVMERTAD 267

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1173344    573 SLFKPSSATWklimEDISEQEGHLQIKLHTPEEN 606
Cdd:PRK15460  268 AVVVPMDAGW----SDVGSWSSLWEISAHTAEGN 297
235kDa-fam super family cl31124
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 170-402 3.27e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


The actual alignment was detected with superfamily member TIGR01612:

Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.96  E-value: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344     170 LVKKLTKPINAvievpSKCKASIIGS-GGRTIRE-ISDAYEVKINV-SKEVNENSYDEDMDDTTSNVSLfgDFESVNLAK 246
Cdd:TIGR01612 1391 LIKKIKDDINL-----EECKSKIESTlDDKDIDEcIKKIKELKNHIlSEESNIDTYFKNADENNENVLL--LFKNIEMAD 1463

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344     247 AKILAIVKEETKNATIKLVVEDEKYLPYIDVSEFASDEGD------EEVKVQFYKKSGDIVILGPREKAKATKTSIQDyl 320
Cdd:TIGR01612 1464 NKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADknakaiEKNKELFEQYKKDVTELLNKYSALAIKNKFAK-- 1541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344     321 KKLASNLDEEKVKiPSKFQFLIDAEELKEKYNVIVTFPSTPDDElvsfVGLRDKVGEAITYARSSSKSYVVESLDISKAH 400
Cdd:TIGR01612 1542 TKKDSEIIIKEIK-DAHKKFILEAEKSEQKIKEIKKEKFRIEDD----AAKNDKSNKAAIDIQLSLENFENKFLKISDIK 1616


                   ..
gi 1173344     401 SK 402
Cdd:TIGR01612 1617 KK 1618
 
Name Accession Description Interval E-value
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 172-257 1.40e-33

first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411874 [Multi-domain]  Cd Length: 86  Bit Score: 124.44  E-value: 1.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   172 KKLTKPINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMDDTTSNVSLFGDFESVNLAKAKILA 251
Cdd:cd22446    1 KELSPKVTITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNEEGNYDEDDDDETVEISIEGDAEGVELAKKEIEA 80


                 ....*.
gi 1173344   252 IVKEET 257
Cdd:cd22446   81 IVKERT 86
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 632-707 4.77e-30

second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 114.05  E-value: 4.77e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   632 SSKSKMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNAS----KDKTVEVTLTGLEYNLTHAKKYLAAEAK 707
Cdd:cd22447    1 SPKQNLTVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPadedDDTMVEVTITGDEFNVQHAKQRIEEIIS 80
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 711-777 3.00e-29

third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411876  Cd Length: 81  Bit Score: 111.85  E-value: 3.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   711 DIITKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDN--------------EIVTIRGPSRGVNKAHEELKALLD 776
Cdd:cd22448    1 DETTLILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPRENsssndtetkkpqapDEVTIRGGKKGVAEAKQELLELLE 80


                 .
gi 1173344   777 F 777
Cdd:cd22448   81 Y 81
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 940-1008 5.21e-27

sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the sixth one.


Pssm-ID: 411879 [Multi-domain]  Cd Length: 69  Bit Score: 104.84  E-value: 5.21e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   940 VTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKILNEIIRE 1008
Cdd:cd22451    1 ASIDIDIPKEYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGKIRITGARDGVEAATAKILNISDEE 69
KH-I_ScSCP160_rpt5 cd22450
fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 859-935 6.72e-27

fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fifth one.


Pssm-ID: 411878  Cd Length: 80  Bit Score: 105.05  E-value: 6.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   859 SDFVTEVLKIDHKYHKSIVGSGGHILREIISKAGG---EEIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEINKIVKD 935
Cdd:cd22450    1 EDEVTRTIKVDRKYHRTIIGPGGSTLRELISKAGGptdRQEQARLVRFPNQNSESDEVVIRGPKKIVEKIIAEIEKIVEE 80
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1152-1218 1.37e-22

seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the seventh one.


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 92.00  E-value: 1.37e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344  1152 TYAGYVWGADtRRFNMIVGPGGSNIKKIREAADVIINVPRKsDKVNDVVYIRGTKAGVEKAGEMVLK 1218
Cdd:cd22452    1 DFRGWIKVSP-RYFGRIIGPGGSNINQIREKSGCFINVPKK-NKESDVITLRGTKEGVEKAEEMIKK 65
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 780-857 2.75e-21

fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 88.48  E-value: 2.75e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344   780 ENGHKMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKstdpkaqeTGEVELEITGSRQNIKDAAKRVESIVAE 857
Cdd:cd22449    1 ENGYTVKFDVPAKYVPHIIGKKGANINKLREEYGVKIDFEDK--------TGEGNVEIKGSKKNVEEAKKRILSQIDE 70
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 787-853 1.16e-11

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 61.14  E-value: 1.16e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344     787 INVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKSTDPkaqetGEVELEITGSRQNIKDAAKRVES 853
Cdd:pfam00013    4 ILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEG-----NERIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
938-1005 3.31e-11

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 60.00  E-value: 3.31e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344      938 NSVTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKILNEI 1005
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 714-773 4.23e-10

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 56.52  E-value: 4.23e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344     714 TKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRD-----NEIVTIRGPSRGVNKAHEELKA 773
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSesegnERIVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 941-1003 4.53e-10

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 56.52  E-value: 4.53e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344     941 TKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGK--ITITGAPENVEKAEKKILN 1003
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNEriVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
783-855 3.03e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 54.22  E-value: 3.03e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344      783 HKMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKSTDpkaqetgEVELEITGSRQNIKDAAKRVESIV 855
Cdd:smart00322    3 VTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSE-------ERVVEITGPPENVEKAAELILEIL 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 636-704 3.14e-09

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 54.21  E-value: 3.14e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344     636 KMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASKdktvEVTLTGLEYNLTHAKKYLAA 704
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNER----IVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 1168-1218 4.93e-09

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 53.82  E-value: 4.93e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1173344    1168 IVGPGGSNIKKIREAADVIINVPRKSDKVND-VVYIRGTKAGVEKAGEMVLK 1218
Cdd:pfam00013   14 IIGKGGSNIKEIREETGAKIQIPPSESEGNErIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
711-775 7.98e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 53.07  E-value: 7.98e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344      711 DIITKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDNE---IVTIRGPSRGVNKAHEELKALL 775
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSeerVVEITGPPENVEKAAELILEIL 68
KH smart00322
K homology RNA-binding domain;
1168-1220 7.15e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 50.37  E-value: 7.15e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1173344     1168 IVGPGGSNIKKIREAADVIINVPRKSDKvNDVVYIRGTKAGVEKAGEMVLKSL 1220
Cdd:smart00322   17 IIGKGGSTIKKIEEETGVKIDIPGPGSE-ERVVEITGPPENVEKAAELILEIL 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 182-251 8.76e-08

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 49.97  E-value: 8.76e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344     182 IEVPSKCKASIIGSGGRTIREISDAYEVKINVSkevnensyDEDMDDTTSNVSLFGDFESVNLAKAKILA 251
Cdd:pfam00013    4 ILVPSSLVGLIIGKGGSNIKEIREETGAKIQIP--------PSESEGNERIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
633-704 9.31e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 49.99  E-value: 9.31e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173344      633 SKSKMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNaskdktVEVTLTGLEYNLTHAKKYLAA 704
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEE------RVVEITGPPENVEKAAELILE 66
KH smart00322
K homology RNA-binding domain;
176-253 1.53e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 49.60  E-value: 1.53e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344      176 KPINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENsydedmddttSNVSLFGDFESVNLAKAKILAIV 253
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEE----------RVVEITGPPENVEKAAELILEIL 68
PRK13764 PRK13764
ATPase; Provisional
 771-842 2.12e-06

ATPase; Provisional


Pssm-ID: 184311 [Multi-domain]  Cd Length: 602  Bit Score: 52.15  E-value: 2.12e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173344    771 LKALLDFEMENGHKMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDF--LQKSTDPKAQETGEVELEITGSRQ 842
Cdd:PRK13764  469 LPGPVEVEVVSDNKAVVYVPEKDIPKVIGKGGKRIKKIEKKLGIDIDVrpLDEEPGEEAEEGEEVTVEETKKHV 542
KH smart00322
K homology RNA-binding domain;
860-933 2.48e-06

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 46.13  E-value: 2.48e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173344      860 DFVTEVLKIDHKYHKSIVGSGGHILREIiskaggEEIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEINKIV 933
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKI------EEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
 185-291 1.83e-05

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 48.89  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344    185 PSKCKAsIIGSGGRTIREISDAYEVKINVSkevnensydedmDDTTsnVSLFG-DFESVNLAKAKILAIVKE----ETKN 259
Cdd:PRK11824  562 PDKIRD-VIGPGGKTIREITEETGAKIDIE------------DDGT--VKIAAtDGEAAEAAKERIEGITAEpevgEIYE 626

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1173344    260 ATIK------LVVEdekYLPYID----VSEFA-------SD---EGDE-EVKV 291
Cdd:PRK11824  627 GKVVrivdfgAFVE---ILPGKDglvhISEIAdervekvEDvlkEGDEvKVKV 676
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 863-931 2.61e-05

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 43.04  E-value: 2.61e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173344     863 TEVLKIDHKYHKSIVGSGGHILREIiskaggEEIRNKSVDIPNADSENKD--ITVQGPQKFVKKVVEEINK 931
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEI------REETGAKIQIPPSESEGNEriVTITGTPEAVEAAKALIEE 65
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
 943-1008 1.96e-03

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 42.34  E-value: 1.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344    943 TIDIPAERKGALIGPGGIVRRQLESEFN--INLfvpnkdDPSGKITITGA-PENVEKAEKKIlNEIIRE 1008
Cdd:PRK11824  557 TIKIPPDKIRDVIGPGGKTIREITEETGakIDI------EDDGTVKIAATdGEAAEAAKERI-EGITAE 618
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 502-606 2.15e-03

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 42.27  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344    502 ESSVAFVQFGDYYPNDNSILLVA---LTEDEDFKPSI-EEIQASLNKANESLNSLRTKQNNM-----ETKTYEFSEEVQD 572
Cdd:PRK15460  188 ETAQAYVASGEYYWNSGMFLFRAgryLEELKKYRPDIlDACEKAMSAVDPDLDFIRVDEEAFlacpeESVDYAVMERTAD 267

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1173344    573 SLFKPSSATWklimEDISEQEGHLQIKLHTPEEN 606
Cdd:PRK15460  268 AVVVPMDAGW----SDVGSWSSLWEISAHTAEGN 297
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 170-402 3.27e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.96  E-value: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344     170 LVKKLTKPINAvievpSKCKASIIGS-GGRTIRE-ISDAYEVKINV-SKEVNENSYDEDMDDTTSNVSLfgDFESVNLAK 246
Cdd:TIGR01612 1391 LIKKIKDDINL-----EECKSKIESTlDDKDIDEcIKKIKELKNHIlSEESNIDTYFKNADENNENVLL--LFKNIEMAD 1463

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344     247 AKILAIVKEETKNATIKLVVEDEKYLPYIDVSEFASDEGD------EEVKVQFYKKSGDIVILGPREKAKATKTSIQDyl 320
Cdd:TIGR01612 1464 NKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADknakaiEKNKELFEQYKKDVTELLNKYSALAIKNKFAK-- 1541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344     321 KKLASNLDEEKVKiPSKFQFLIDAEELKEKYNVIVTFPSTPDDElvsfVGLRDKVGEAITYARSSSKSYVVESLDISKAH 400
Cdd:TIGR01612 1542 TKKDSEIIIKEIK-DAHKKFILEAEKSEQKIKEIKKEKFRIEDD----AAKNDKSNKAAIDIQLSLENFENKFLKISDIK 1616


                   ..
gi 1173344     401 SK 402
Cdd:TIGR01612 1617 KK 1618
 
Name Accession Description Interval E-value
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 172-257 1.40e-33

first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411874 [Multi-domain]  Cd Length: 86  Bit Score: 124.44  E-value: 1.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   172 KKLTKPINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMDDTTSNVSLFGDFESVNLAKAKILA 251
Cdd:cd22446    1 KELSPKVTITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNEEGNYDEDDDDETVEISIEGDAEGVELAKKEIEA 80


                 ....*.
gi 1173344   252 IVKEET 257
Cdd:cd22446   81 IVKERT 86
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 632-707 4.77e-30

second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 114.05  E-value: 4.77e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   632 SSKSKMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNAS----KDKTVEVTLTGLEYNLTHAKKYLAAEAK 707
Cdd:cd22447    1 SPKQNLTVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPadedDDTMVEVTITGDEFNVQHAKQRIEEIIS 80
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 711-777 3.00e-29

third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411876  Cd Length: 81  Bit Score: 111.85  E-value: 3.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   711 DIITKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDN--------------EIVTIRGPSRGVNKAHEELKALLD 776
Cdd:cd22448    1 DETTLILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPRENsssndtetkkpqapDEVTIRGGKKGVAEAKQELLELLE 80


                 .
gi 1173344   777 F 777
Cdd:cd22448   81 Y 81
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 940-1008 5.21e-27

sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the sixth one.


Pssm-ID: 411879 [Multi-domain]  Cd Length: 69  Bit Score: 104.84  E-value: 5.21e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   940 VTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKILNEIIRE 1008
Cdd:cd22451    1 ASIDIDIPKEYHRAIIGKGGAVLRELEAETGCRIQVPKKDDPSGKIRITGARDGVEAATAKILNISDEE 69
KH-I_ScSCP160_rpt5 cd22450
fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 859-935 6.72e-27

fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fifth one.


Pssm-ID: 411878  Cd Length: 80  Bit Score: 105.05  E-value: 6.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   859 SDFVTEVLKIDHKYHKSIVGSGGHILREIISKAGG---EEIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEINKIVKD 935
Cdd:cd22450    1 EDEVTRTIKVDRKYHRTIIGPGGSTLRELISKAGGptdRQEQARLVRFPNQNSESDEVVIRGPKKIVEKIIAEIEKIVEE 80
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1152-1218 1.37e-22

seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the seventh one.


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 92.00  E-value: 1.37e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344  1152 TYAGYVWGADtRRFNMIVGPGGSNIKKIREAADVIINVPRKsDKVNDVVYIRGTKAGVEKAGEMVLK 1218
Cdd:cd22452    1 DFRGWIKVSP-RYFGRIIGPGGSNINQIREKSGCFINVPKK-NKESDVITLRGTKEGVEKAEEMIKK 65
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 780-857 2.75e-21

fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 88.48  E-value: 2.75e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344   780 ENGHKMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKstdpkaqeTGEVELEITGSRQNIKDAAKRVESIVAE 857
Cdd:cd22449    1 ENGYTVKFDVPAKYVPHIIGKKGANINKLREEYGVKIDFEDK--------TGEGNVEIKGSKKNVEEAKKRILSQIDE 70
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 787-853 1.16e-11

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 61.14  E-value: 1.16e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344     787 INVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKSTDPkaqetGEVELEITGSRQNIKDAAKRVES 853
Cdd:pfam00013    4 ILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEG-----NERIVTITGTPEAVEAAKALIEE 65
KH smart00322
K homology RNA-binding domain;
938-1005 3.31e-11

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 60.00  E-value: 3.31e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344      938 NSVTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKILNEI 1005
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 173-254 9.77e-11

second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 58.97  E-value: 9.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   173 KLTKPInavievPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMDDTTSNVSLFGDFESVNLAKAKILAI 252
Cdd:cd22447    5 NLTVPI------PASTRARIIGKKGANLKQIREKTGVRIDIPPRDADAAPADEDDDTMVEVTITGDEFNVQHAKQRIEEI 78


                 ..
gi 1173344   253 VK 254
Cdd:cd22447   79 IS 80
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 784-857 1.68e-10

fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourteenth one.


Pssm-ID: 411845 [Multi-domain]  Cd Length: 72  Bit Score: 57.99  E-value: 1.68e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173344   784 KMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFlqkstdPKAQETGEVELEITGSRQNIKDAAKRVESIVAE 857
Cdd:cd22417    2 TLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQF------PDKGDENDDEITITGYEKNAEAAKDAILKIVQE 69
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 942-1002 1.81e-10

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 57.69  E-value: 1.81e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   942 KTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSG--KITITGAPENVEKAEKKIL 1002
Cdd:cd00105    1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGerVVTITGTPEAVEKAKELIE 63
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 716-776 3.86e-10

fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourteenth one.


Pssm-ID: 411845 [Multi-domain]  Cd Length: 72  Bit Score: 56.83  E-value: 3.86e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   716 ELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDNE----IVTIRGPSRGVNKAHEELKALLD 776
Cdd:cd22417    4 TVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDenddEITITGYEKNAEAAKDAILKIVQ 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 714-773 4.23e-10

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 56.52  E-value: 4.23e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344     714 TKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRD-----NEIVTIRGPSRGVNKAHEELKA 773
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSesegnERIVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 941-1003 4.53e-10

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 56.52  E-value: 4.53e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344     941 TKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGK--ITITGAPENVEKAEKKILN 1003
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNEriVTITGTPEAVEAAKALIEE 65
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 786-852 6.72e-10

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 56.15  E-value: 6.72e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344   786 VINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFlqkstDPKAQETGEVELEITGSRQNIKDAAKRVE 852
Cdd:cd00105    2 EIEVPSELVGLIIGKGGSTIKEIEEETGARIQI-----PKEGEGSGERVVTITGTPEAVEKAKELIE 63
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 714-776 2.30e-09

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 54.50  E-value: 2.30e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173344   714 TKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDNE---IVTIRGPSRGVNKAHEELKALLD 776
Cdd:cd02394    3 FTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEAnsdEIRIEGSPEGVKKAKAEILELVD 68
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 714-774 2.48e-09

seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the seventh one.


Pssm-ID: 411838  Cd Length: 67  Bit Score: 54.59  E-value: 2.48e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   714 TKELIVPVKFHGSLIGPHGTYRNRLQEKYN-VFINFP---RDNEIVTIRGPSRGVNKAHEELKAL 774
Cdd:cd22410    3 TKDIIIEQRFHRTIIGQKGEKIREIRDKFPqVQITFPdpgSKSDVVTLRGPKDEVDKCYKYLKKL 67
KH smart00322
K homology RNA-binding domain;
783-855 3.03e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 54.22  E-value: 3.03e-09
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344      783 HKMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKSTDpkaqetgEVELEITGSRQNIKDAAKRVESIV 855
Cdd:smart00322    3 VTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSE-------ERVVEITGPPENVEKAAELILEIL 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 636-704 3.14e-09

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 54.21  E-value: 3.14e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344     636 KMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASKdktvEVTLTGLEYNLTHAKKYLAA 704
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIQIPPSESEGNER----IVTITGTPEAVEAAKALIEE 65
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 1168-1218 4.93e-09

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 53.82  E-value: 4.93e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1173344    1168 IVGPGGSNIKKIREAADVIINVPRKSDKVND-VVYIRGTKAGVEKAGEMVLK 1218
Cdd:pfam00013   14 IIGKGGSNIKEIREETGAKIQIPPSESEGNErIVTITGTPEAVEAAKALIEE 65
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 939-1003 6.06e-09

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 53.34  E-value: 6.06e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   939 SVTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKILN 1003
Cdd:cd02394    1 MAFTTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILE 65
KH smart00322
K homology RNA-binding domain;
711-775 7.98e-09

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 53.07  E-value: 7.98e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344      711 DIITKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDNE---IVTIRGPSRGVNKAHEELKALL 775
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSeerVVEITGPPENVEKAAELILEIL 68
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 715-772 9.16e-09

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 52.69  E-value: 9.16e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   715 KELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDNE-----IVTIRGPSRGVNKAHEELK 772
Cdd:cd00105    1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEgsgerVVTITGTPEAVEKAKELIE 63
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 940-1013 1.31e-08

thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the thirteenth one.


Pssm-ID: 411844 [Multi-domain]  Cd Length: 78  Bit Score: 53.00  E-value: 1.31e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344   940 VTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKILN---EIIRENFDRE 1013
Cdd:cd22416    2 VTEEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPAELQSDIIKITGPPANVERAKAALLErvkELEAEKEDRE 78
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 1167-1217 3.29e-08

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 51.42  E-value: 3.29e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1173344  1167 MIVGPGGSNIKKIREAADVIINVPrKSDKVNDVVYIRGTKAGVEKAGEMVL 1217
Cdd:cd02394   15 HIIGKGGANIKRIREESGVSIRIP-DDEANSDEIRIEGSPEGVKKAKAEIL 64
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 941-1002 4.52e-08

eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the eighth one.


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 50.66  E-value: 4.52e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173344   941 TKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKIL 1002
Cdd:cd22411    1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 181-250 6.95e-08

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 50.37  E-value: 6.95e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   181 VIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKevnensydEDMDDTTSNVSLFGDFESVNLAKAKIL 250
Cdd:cd00105    2 EIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPK--------EGEGSGERVVTITGTPEAVEKAKELIE 63
KH smart00322
K homology RNA-binding domain;
1168-1220 7.15e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 50.37  E-value: 7.15e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1173344     1168 IVGPGGSNIKKIREAADVIINVPRKSDKvNDVVYIRGTKAGVEKAGEMVLKSL 1220
Cdd:smart00322   17 IIGKGGSTIKKIEEETGVKIDIPGPGSE-ERVVEITGPPENVEKAAELILEIL 68
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 182-251 8.76e-08

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 49.97  E-value: 8.76e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344     182 IEVPSKCKASIIGSGGRTIREISDAYEVKINVSkevnensyDEDMDDTTSNVSLFGDFESVNLAKAKILA 251
Cdd:pfam00013    4 ILVPSSLVGLIIGKGGSNIKEIREETGAKIQIP--------PSESEGNERIVTITGTPEAVEAAKALIEE 65
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 943-1008 8.79e-08

fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourteenth one.


Pssm-ID: 411845 [Multi-domain]  Cd Length: 72  Bit Score: 50.28  E-value: 8.79e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344   943 TIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDP-SGKITITGAPENVEKAEKKILnEIIRE 1008
Cdd:cd22417    4 TVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDEnDDEITITGYEKNAEAAKDAIL-KIVQE 69
KH smart00322
K homology RNA-binding domain;
633-704 9.31e-08

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 49.99  E-value: 9.31e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173344      633 SKSKMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNaskdktVEVTLTGLEYNLTHAKKYLAA 704
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEE------RVVEITGPPENVEKAAELILE 66
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 1161-1217 1.08e-07

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 49.99  E-value: 1.08e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344  1161 DTRRFNMIVGPGGSNIKKIREAADVIINVPRKSDKVND-VVYIRGTKAGVEKAGEMVL 1217
Cdd:cd00105    6 PSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGErVVTITGTPEAVEKAKELIE 63
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 638-702 1.44e-07

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 49.60  E-value: 1.44e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   638 TVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASKdktvEVTLTGLEYNLTHAKKYL 702
Cdd:cd00105    2 EIEVPSELVGLIIGKGGSTIKEIEEETGARIQIPKEGEGSGER----VVTITGTPEAVEKAKELI 62
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1167-1218 1.45e-07

fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourteenth one.


Pssm-ID: 411845 [Multi-domain]  Cd Length: 72  Bit Score: 49.90  E-value: 1.45e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1173344  1167 MIVGPGGSNIKKIREAADVIINVPRKSDKVNDVVYIRGTKAGVEKAGEMVLK 1218
Cdd:cd22417   14 KIIGRKGAVITKLRDDHDVNIQFPDKGDENDDEITITGYEKNAEAAKDAILK 65
KH smart00322
K homology RNA-binding domain;
176-253 1.53e-07

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 49.60  E-value: 1.53e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344      176 KPINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENsydedmddttSNVSLFGDFESVNLAKAKILAIV 253
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIDIPGPGSEE----------RVVEITGPPENVEKAAELILEIL 68
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 784-856 1.71e-07

second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 49.72  E-value: 1.71e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173344   784 KMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKSTD--PKAQETGE-VELEITGSRQNIKDAAKRVESIVA 856
Cdd:cd22447    5 NLTVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDADaaPADEDDDTmVEVTITGDEFNVQHAKQRIEEIIS 80
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 939-1001 1.78e-07

second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the second one.


Pssm-ID: 411834 [Multi-domain]  Cd Length: 75  Bit Score: 49.62  E-value: 1.78e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   939 SVTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKI 1001
Cdd:cd22406    4 QASVTVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQEDNSDEIKITGTKEGIEKARHEI 66
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 861-934 3.70e-07

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 48.34  E-value: 3.70e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173344   861 FVTEVLKIDHKYHKSIVGSGGHILREIiskaggEEIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEINKIVK 934
Cdd:cd02394    1 MAFTTIEIDPKFHGHIIGKGGANIKRI------REESGVSIRIPDDEANSDEIRIEGSPEGVKKAKAEILELVD 68
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 786-855 4.00e-07

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 48.34  E-value: 4.00e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   786 VINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFlqkstdpKAQETGEVELEITGSRQNIKDAAKRVESIV 855
Cdd:cd02394    5 TIEIDPKFHGHIIGKGGANIKRIREESGVSIRI-------PDDEANSDEIRIEGSPEGVKKAKAEILELV 67
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 180-254 1.11e-06

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 47.18  E-value: 1.11e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   180 AVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEvNENSydedmddttSNVSLFGDFESVNLAKAKILAIVK 254
Cdd:cd02394    4 TTIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDD-EANS---------DEIRIEGSPEGVKKAKAEILELVD 68
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 712-773 1.46e-06

seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the seventh one.


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 46.54  E-value: 1.46e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   712 IITKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPR---DNEIVTIRGPSRGVNKAHEELKA 773
Cdd:cd22452    1 DFRGWIKVSPRYFGRIIGPGGSNINQIREKSGCFINVPKknkESDVITLRGTKEGVEKAEEMIKK 65
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 787-855 2.08e-06

first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411824 [Multi-domain]  Cd Length: 68  Bit Score: 46.48  E-value: 2.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   787 INVPAEHVPRIIGKNGDNINDIRAEYGVemdFLQKSTDPKAQetGEVELEITGSRQNIKDAAKRVESIV 855
Cdd:cd22396    5 YKVPDKMVGLIIGRGGEQINRLQAESGA---KIQIAPDSGGL--PERPCTLTGTPDAIETAKRLIDQIV 68
PRK13764 PRK13764
ATPase; Provisional
 771-842 2.12e-06

ATPase; Provisional


Pssm-ID: 184311 [Multi-domain]  Cd Length: 602  Bit Score: 52.15  E-value: 2.12e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173344    771 LKALLDFEMENGHKMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDF--LQKSTDPKAQETGEVELEITGSRQ 842
Cdd:PRK13764  469 LPGPVEVEVVSDNKAVVYVPEKDIPKVIGKGGKRIKKIEKKLGIDIDVrpLDEEPGEEAEEGEEVTVEETKKHV 542
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 862-924 2.44e-06

ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the ninth one.


Pssm-ID: 411840  Cd Length: 70  Bit Score: 46.13  E-value: 2.44e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   862 VTEVLKIDHKYHKSIVGSGGHILREIISKAGGEEIRnksvdIPNADSENKDITVQGPQKFVKK 924
Cdd:cd22412    2 VEVEVEIPAKLHNSLIGAKGRLIRSIMEECGGVHIH-----FPPEGSGSDKVTIRGPKEDVEK 59
KH smart00322
K homology RNA-binding domain;
860-933 2.48e-06

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 46.13  E-value: 2.48e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173344      860 DFVTEVLKIDHKYHKSIVGSGGHILREIiskaggEEIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEINKIV 933
Cdd:smart00322    1 DPVTIEVLIPADKVGLIIGKGGSTIKKI------EEETGVKIDIPGPGSEERVVEITGPPENVEKAAELILEIL 68
KH-I_FUBP_rpt3 cd22398
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 784-855 2.71e-06

third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411826 [Multi-domain]  Cd Length: 67  Bit Score: 46.10  E-value: 2.71e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173344   784 KMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFlqKSTDPKAQETGEVeleITGSRQNIKDAAKRVESIV 855
Cdd:cd22398    1 GMEVPVPRFAVGVVIGKGGEMIKKIQNETGARVQF--KPDDGNSPDRICV---ITGPPDQVQHAARMIQELI 67
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 636-700 3.14e-06

fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourteenth one.


Pssm-ID: 411845 [Multi-domain]  Cd Length: 72  Bit Score: 46.05  E-value: 3.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   636 KMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASkdktvEVTLTGLEYNLTHAKK 700
Cdd:cd22417    2 TLTVEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDENDD-----EITITGYEKNAEAAKD 61
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1168-1217 4.40e-06

eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the eighth one.


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 45.27  E-value: 4.40e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1173344  1168 IVGPGGSNIKKIREAADVIINVPrKSDKVNDVVYIRGTKAGVEKAGEMVL 1217
Cdd:cd22411   14 IIGKGGATIKKIREETNTRIDLP-EENSDSDVITITGKKEDVEKARERIL 62
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 941-1002 5.21e-06

fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourth one.


Pssm-ID: 411836 [Multi-domain]  Cd Length: 62  Bit Score: 44.85  E-value: 5.21e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173344   941 TKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKIL 1002
Cdd:cd22408    1 TVSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDSDSETITLRGPADKLGAALTLVY 62
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 182-256 6.29e-06

fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourteenth one.


Pssm-ID: 411845 [Multi-domain]  Cd Length: 72  Bit Score: 45.28  E-value: 6.29e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   182 IEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSydedmddttSNVSLFGDFESVNLAKAKILAIVKEE 256
Cdd:cd22417    5 VEVDPKYHPKIIGRKGAVITKLRDDHDVNIQFPDKGDEND---------DEITITGYEKNAEAAKDAILKIVQEL 70
KH-I_Vigilin_rpt14 cd22417
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 866-938 6.61e-06

fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourteenth one.


Pssm-ID: 411845 [Multi-domain]  Cd Length: 72  Bit Score: 44.89  E-value: 6.61e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344   866 LKIDHKYHKSIVGSGGhilrEIISKaggeeIRNK---SVDIPNADSENKD-ITVQGPQKFVKKVVEEINKIVKDAEN 938
Cdd:cd22417    5 VEVDPKYHPKIIGRKG----AVITK-----LRDDhdvNIQFPDKGDENDDeITITGYEKNAEAAKDAILKIVQELES 72
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 181-253 7.38e-06

third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411876  Cd Length: 81  Bit Score: 45.21  E-value: 7.38e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173344   181 VIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMDDTTSN-VSLFGDFESVNLAKAKILAIV 253
Cdd:cd22448    6 ILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPRENSSSNDTETKKPQAPDeVTIRGGKKGVAEAKQELLELL 79
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 1164-1216 9.42e-06

tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the tenth one.


Pssm-ID: 411841 [Multi-domain]  Cd Length: 66  Bit Score: 44.56  E-value: 9.42e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1173344  1164 RFnmIVGPGGSNIKKIREAADVIINVPRKSDKVNDVVYIRGTKAGVEKAGEMV 1216
Cdd:cd22413   15 RF--LIGRGGANIRKIRDNTGARIIFPTARDEDQELITIIGTKEAVEKAKEEL 65
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 636-708 1.22e-05

fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 44.18  E-value: 1.22e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   636 KMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIpneennnASKDKTVEVTLTGLEYNLTHAKKYLAAEAKK 708
Cdd:cd22449    5 TVKFDVPAKYVPHIIGKKGANINKLREEYGVKIDF-------EDKTGEGNVEIKGSKKNVEEAKKRILSQIDE 70
KH-I_FUBP_rpt2 cd22397
second type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 787-851 1.70e-05

second type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411825 [Multi-domain]  Cd Length: 69  Bit Score: 43.77  E-value: 1.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   787 INVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKSTDPKAQETgevELEITGSRQNIKDAAKRV 851
Cdd:cd22397    4 IMIPGNKVGLIIGKGGETIKQLQERAGVKMVMIQDGPQPTGQDK---PLRITGDPQKVQRAKELV 65
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 712-774 1.75e-05

ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the ninth one.


Pssm-ID: 411840  Cd Length: 70  Bit Score: 43.82  E-value: 1.75e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344   712 IITKELIVPVKFHGSLIGPHGTYRNRLQEKYN-VFINFPRD---NEIVTIRGPSRGVNKAHEELKAL 774
Cdd:cd22412    1 IVEVEVEIPAKLHNSLIGAKGRLIRSIMEECGgVHIHFPPEgsgSDKVTIRGPKEDVEKAKKQLLEL 67
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
 185-291 1.83e-05

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 48.89  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344    185 PSKCKAsIIGSGGRTIREISDAYEVKINVSkevnensydedmDDTTsnVSLFG-DFESVNLAKAKILAIVKE----ETKN 259
Cdd:PRK11824  562 PDKIRD-VIGPGGKTIREITEETGAKIDIE------------DDGT--VKIAAtDGEAAEAAKERIEGITAEpevgEIYE 626

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1173344    260 ATIK------LVVEdekYLPYID----VSEFA-------SD---EGDE-EVKV 291
Cdd:PRK11824  627 GKVVrivdfgAFVE---ILPGKDglvhISEIAdervekvEDvlkEGDEvKVKV 676
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 863-931 2.61e-05

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 43.04  E-value: 2.61e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173344     863 TEVLKIDHKYHKSIVGSGGHILREIiskaggEEIRNKSVDIPNADSENKD--ITVQGPQKFVKKVVEEINK 931
Cdd:pfam00013    1 TVEILVPSSLVGLIIGKGGSNIKEI------REETGAKIQIPPSESEGNEriVTITGTPEAVEAAKALIEE 65
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 940-1006 2.88e-05

second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 43.56  E-value: 2.88e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344   940 VTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKD----------DPSGKITITGAPENVEKAEKKIlNEII 1006
Cdd:cd22447    4 QNLTVPIPASTRARIIGKKGANLKQIREKTGVRIDIPPRDadaapadeddDTMVEVTITGDEFNVQHAKQRI-EEII 79
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1167-1217 2.96e-05

fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourth one.


Pssm-ID: 411836 [Multi-domain]  Cd Length: 62  Bit Score: 42.93  E-value: 2.96e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 1173344  1167 MIVGPGGSNIKKIREAADVIINVPRKSDKVNDVVyIRGTKAGVEKAGEMVL 1217
Cdd:cd22408   13 FVIGPRGSTIQEILEETGCSVEVPPNDSDSETIT-LRGPADKLGAALTLVY 62
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1167-1212 4.81e-05

second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the second one.


Pssm-ID: 411834 [Multi-domain]  Cd Length: 75  Bit Score: 42.68  E-value: 4.81e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 1173344  1167 MIVGPGGSNIKKIREAADVIINVPRKSDKvNDVVYIRGTKAGVEKA 1212
Cdd:cd22406   18 FILGKKGKKLQELELKTATKIVIPRQEDN-SDEIKITGTKEGIEKA 62
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 860-933 5.54e-05

third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411876  Cd Length: 81  Bit Score: 42.90  E-value: 5.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   860 DFVTEVLKIDHKYHKSIVGSGGHILREIiskaggEEIRNKSVDIPNADSENKD-----------ITVQGPQKFVKKVVEE 928
Cdd:cd22448    1 DETTLILKIPVQFHGSLIGQQGKYVNRL------QEKYGVKINFPRENSSSNDtetkkpqapdeVTIRGGKKGVAEAKQE 74


                 ....*
gi 1173344   929 INKIV 933
Cdd:cd22448   75 LLELL 79
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 940-1002 5.68e-05

seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the seventh one.


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 42.31  E-value: 5.68e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   940 VTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKIL 1002
Cdd:cd22452    2 FRGWIKVSPRYFGRIIGPGGSNINQIREKSGCFINVPKKNKESDVITLRGTKEGVEKAEEMIK 64
KH-I_Vigilin_rpt9 cd22412
ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 940-1002 6.03e-05

ninth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the ninth one.


Pssm-ID: 411840  Cd Length: 70  Bit Score: 42.28  E-value: 6.03e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173344   940 VTKTIDIPAERKGALIGPGGIVRRQLESEFN-INLFVPNKDDPSGKITITGAPENVEKAEKKIL 1002
Cdd:cd22412    2 VEVEVEIPAKLHNSLIGAKGRLIRSIMEECGgVHIHFPPEGSGSDKVTIRGPKEDVEKAKKQLL 65
KH-I_DDX43_DDX53 cd22430
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ...
 192-255 6.10e-05

type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53) and similar proteins; DDX43 (also called cancer/testis antigen 13, or DEAD box protein HAGE, or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 (also called cancer-associated gene protein, or cancer/testis antigen 26, or DEAD box protein CAGE) shows high expression level in various tumors and is involved in anti-cancer drug resistance. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation.


Pssm-ID: 411858 [Multi-domain]  Cd Length: 66  Bit Score: 42.27  E-value: 6.10e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173344   192 IIGSGGRTIREISDAYEVKINVSKEVNENSydedmddttsnVSLFGDFESVNLAKAKILAIVKE 255
Cdd:cd22430   14 VIGRGGSKIRELEESTGSKIKIIKGGQEAE-----------VKIFGSDEAQQKAKELIDELVGR 66
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 637-699 6.50e-05

fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourth one.


Pssm-ID: 411836 [Multi-domain]  Cd Length: 62  Bit Score: 41.77  E-value: 6.50e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   637 MTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNAskdktvEVTLTGLEYNLTHAK 699
Cdd:cd22408    2 VSVEVPKSQHRFVIGPRGSTIQEILEETGCSVEVPPNDSDSE------TITLRGPADKLGAAL 58
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 938-1001 6.98e-05

tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the tenth one.


Pssm-ID: 411841 [Multi-domain]  Cd Length: 66  Bit Score: 41.86  E-value: 6.98e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   938 NSVTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGK-ITITGAPENVEKAEKKI 1001
Cdd:cd22413    1 NSFTVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPTARDEDQElITIIGTKEAVEKAKEEL 65
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1161-1218 7.45e-05

thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the thirteenth one.


Pssm-ID: 411844 [Multi-domain]  Cd Length: 78  Bit Score: 42.22  E-value: 7.45e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344  1161 DTRRFnmIVGPGGSNIKKIREAADVIINVPRKSDKvNDVVYIRGTKAGVEKAGEMVLK 1218
Cdd:cd22416   11 DLHRF--IIGQKGADVRKMMDEFDVNISIPPAELQ-SDIIKITGPPANVERAKAALLE 65
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
 631-684 7.54e-05

first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the first one.


Pssm-ID: 411856 [Multi-domain]  Cd Length: 74  Bit Score: 41.94  E-value: 7.54e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1173344   631 PSSKSKMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASKDKTV 684
Cdd:cd22428    1 GSRQIEIEMKVPREAVGLIIGRQGATIKQIQKETGARIDFKDEGSGGELPERVL 54
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 713-771 8.54e-05

thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the thirteenth one.


Pssm-ID: 411844 [Multi-domain]  Cd Length: 78  Bit Score: 42.22  E-value: 8.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173344   713 ITKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDN---EIVTIRGPSRGVNKAHEEL 771
Cdd:cd22416    2 VTEEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPAElqsDIIKITGPPANVERAKAAL 63
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 863-930 8.87e-05

eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the eighth one.


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 41.42  E-value: 8.87e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344   863 TEVLKIDHKYHKSIVGSGGHILREIiskaggEEIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEIN 930
Cdd:cd22411    1 SIKVPIFKQFHKNIIGKGGATIKKI------REETNTRIDLPEENSDSDVITITGKKEDVEKARERIL 62
KH-I_TDRKH_rpt2 cd22429
second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
 177-256 9.89e-05

second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the second one.


Pssm-ID: 411857 [Multi-domain]  Cd Length: 82  Bit Score: 41.94  E-value: 9.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   177 PINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVnensydEDMDDTTSNVSLFGDFESVNLAKAKILAIVKEE 256
Cdd:cd22429    1 IITEELHVPQRAVGRIIGRGGETIRSICRTSGAKVKCDRES------DDTLDLVRLITITGTKKEVDAAKSLILEKVSEE 74
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 638-700 1.23e-04

eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the eighth one.


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 41.03  E-value: 1.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   638 TVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNaskdktVEVTLTGLEYNLTHAKK 700
Cdd:cd22411    3 KVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENSDS------DVITITGKKEDVEKARE 59
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 787-857 1.34e-04

sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the sixth one.


Pssm-ID: 411879 [Multi-domain]  Cd Length: 69  Bit Score: 41.29  E-value: 1.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173344   787 INVPAEHVPRIIGKNGDNINDIRAEYGVEMdFLQKSTDPKAQetgeveLEITGSRQNIKDAAKRVESIVAE 857
Cdd:cd22451    5 IDIPKEYHRAIIGKGGAVLRELEAETGCRI-QVPKKDDPSGK------IRITGARDGVEAATAKILNISDE 68
KH-I_IGF2BP_rpt4 cd22403
fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
 180-249 1.66e-04

fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/CRD-BP/VICKZ1, IGF2BP2/IMP-2/VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the fourth one.


Pssm-ID: 411831 [Multi-domain]  Cd Length: 66  Bit Score: 41.07  E-value: 1.66e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   180 AVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMddttsnVSLFGDFESVNLAKAKI 249
Cdd:cd22403    2 TEIRVPSSMVGRIIGKGGQNVRELQRLTGAIIKLPRDQTPDEGDEVP------VEIIGNFYATQSAQRRI 65
KH-I_ScSCP160_rpt5 cd22450
fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 710-777 1.71e-04

fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fifth one.


Pssm-ID: 411878  Cd Length: 80  Bit Score: 41.11  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   710 ADIITKELIVPVKFHGSLIGPHGTyrnRLQE------------KYNVFINFPRDNE---IVTIRGPSRGVNKAHEELKAL 774
Cdd:cd22450    1 EDEVTRTIKVDRKYHRTIIGPGGS---TLREliskaggptdrqEQARLVRFPNQNSesdEVVIRGPKKIVEKIIAEIEKI 77


                 ...
gi 1173344   775 LDF 777
Cdd:cd22450   78 VEE 80
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1163-1212 1.75e-04

seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the seventh one.


Pssm-ID: 411838  Cd Length: 67  Bit Score: 40.72  E-value: 1.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1173344  1163 RRFN-MIVGPGGSNIKKIREA-ADVIINVPRKSDKvNDVVYIRGTKAGVEKA 1212
Cdd:cd22410   10 QRFHrTIIGQKGEKIREIRDKfPQVQITFPDPGSK-SDVVTLRGPKDEVDKC 60
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 632-690 2.13e-04

first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411874 [Multi-domain]  Cd Length: 86  Bit Score: 41.24  E-value: 2.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   632 SSKSKMTVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNAS----KDKTVEVTLTG 690
Cdd:cd22446    4 SPKVTITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNEEGNYdeddDDETVEISIEG 66
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
 192-255 2.49e-04

type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.


Pssm-ID: 411803 [Multi-domain]  Cd Length: 70  Bit Score: 40.54  E-value: 2.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   192 IIGSGGRTIREISDAYEVKINVSkevnensydedmDDTTsnVSLFG-DFESVNLAKAKILAIVKE 255
Cdd:cd02393   18 VIGPGGKTIRAIIEETGAKIDIE------------DDGT--VTIFAtDKESAEAAKAMIEDIVAE 68
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 182-255 2.50e-04

fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 40.33  E-value: 2.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173344   182 IEVPSKCKASIIGSGGRTIREISDAYEVKINVskevnensydedmDDTTS--NVSLFGDFESVNLAKAKILAIVKE 255
Cdd:cd22449    8 FDVPAKYVPHIIGKKGANINKLREEYGVKIDF-------------EDKTGegNVEIKGSKKNVEEAKKRILSQIDE 70
KH-I_Vigilin_rpt7 cd22410
seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 868-932 3.00e-04

seventh type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the seventh one.


Pssm-ID: 411838  Cd Length: 67  Bit Score: 40.34  E-value: 3.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   868 IDHKYHKSIVGSGGHILREIISKaggeeIRNKSVDIPNADSENKDITVQGPQKFVKKVVEEINKI 932
Cdd:cd22410    8 IEQRFHRTIIGQKGEKIREIRDK-----FPQVQITFPDPGSKSDVVTLRGPKDEVDKCYKYLKKL 67
KH-I_FUBP3_rpt1 cd22480
first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
 940-1006 3.13e-04

first type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411908 [Multi-domain]  Cd Length: 71  Bit Score: 40.27  E-value: 3.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   940 VTKTIDIPAERKGALIGPGG--IVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAeKKILNEII 1006
Cdd:cd22480    1 ITEEYKVPDKMVGFIIGRGGeqISRIQLESGCKIQIAPDSGGMPERPCVLTGTPESIEQA-KRLLGQIV 68
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 940-1003 3.37e-04

fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fifteenth one.


Pssm-ID: 411846 [Multi-domain]  Cd Length: 69  Bit Score: 39.94  E-value: 3.37e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173344   940 VTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVP--NKDDPSgKITITGAPENVEKAEKKILN 1003
Cdd:cd22418    1 VTEEVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPrsGDADPN-LVTITGLEENVEECKDHLLN 65
KH-I_NOVA_rpt3 cd09031
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ...
 940-1005 3.39e-04

third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411807 [Multi-domain]  Cd Length: 71  Bit Score: 40.25  E-value: 3.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   940 VTKTIDIPAERKGALIGPGG--IVRRQLESEFNINL-----FVPNKDDPsgKITITGAPENVEKAEKKILNEI 1005
Cdd:cd09031    1 TVIELEVPENLVGAILGKGGktLVEIQELTGARIQIskkgeFVPGTRNR--KVTITGTPAAVQAAQYLIEQRI 71
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1168-1222 3.56e-04

fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 39.95  E-value: 3.56e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 1173344  1168 IVGPGGSNIKKIREAADVIINVPRKSDKVNdvVYIRGTKAGVEKAGEMVLKSLRR 1222
Cdd:cd22449   18 IIGKKGANINKLREEYGVKIDFEDKTGEGN--VEIKGSKKNVEEAKKRILSQIDE 70
KH-I_ScSCP160_rpt2 cd22447
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1160-1216 3.79e-04

second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411875 [Multi-domain]  Cd Length: 80  Bit Score: 40.48  E-value: 3.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173344  1160 ADTRRFnmIVGPGGSNIKKIREAADVIINVPRKSDKVNDV---------VYIRGTKAGVEKAGEMV 1216
Cdd:cd22447   12 ASTRAR--IIGKKGANLKQIREKTGVRIDIPPRDADAAPAdedddtmveVTITGDEFNVQHAKQRI 75
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
 182-253 3.80e-04

first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the first one.


Pssm-ID: 411856 [Multi-domain]  Cd Length: 74  Bit Score: 40.01  E-value: 3.80e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173344   182 IEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEVNENSYDEDMddttsnVSLFGDFESVNLAKAKILAIV 253
Cdd:cd22428    9 MKVPREAVGLIIGRQGATIKQIQKETGARIDFKDEGSGGELPERV------LLIQGNPVQAQRAEEAIHQII 74
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 638-702 3.83e-04

fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fifteenth one.


Pssm-ID: 411846 [Multi-domain]  Cd Length: 69  Bit Score: 39.94  E-value: 3.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   638 TVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASKdktveVTLTGLEYNLTHAKKYL 702
Cdd:cd22418    4 EVEIDSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGDADPNL-----VTITGLEENVEECKDHL 63
KH-I_MASK cd22404
type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family ...
 786-848 4.41e-04

type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family includes Drosophila melanogaster ankyrin repeat and KH domain-containing protein Mask, and its mammalian homologues Mask1/ANKHD1 and Mask2/ANKRD17. Mask, also called multiple ankyrin repeat single KH domain-containing protein, is a large ankyrin repeat and KH domain-containing protein involved in Drosophila receptor tyrosine kinase signaling. It acts as a mediator of receptor tyrosine kinase (RTK) signaling and may act either downstream of MAPK or transduce signaling through a parallel branch of the RTK pathway. Mask is required for the development and organization of indirect flight muscle sarcomeres by regulating the formation of M line and H zone and the correct assembly of thick and thin filaments in the sarcomere. Mask1/ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. Mask2/ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


Pssm-ID: 411832 [Multi-domain]  Cd Length: 71  Bit Score: 39.89  E-value: 4.41e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   786 VINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFlqkstDPKAQETGEVELEITGSRQNIKDAA 848
Cdd:cd22404    4 KVTVPNSAISRVIGRGGCNINAIREVSGAHIEI-----DKQKGEQGDRRITIKGSADATRQAA 61
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 785-852 4.83e-04

fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourth one.


Pssm-ID: 411836 [Multi-domain]  Cd Length: 62  Bit Score: 39.46  E-value: 4.83e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   785 MVINVPAEHVPRIIGKNGDNINDIRAEYG--VEMdflqkstdPKAQETGEvELEITGSRQNIKDAAKRVE 852
Cdd:cd22408    2 VSVEVPKSQHRFVIGPRGSTIQEILEETGcsVEV--------PPNDSDSE-TITLRGPADKLGAALTLVY 62
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 714-772 5.09e-04

third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the third one.


Pssm-ID: 411835 [Multi-domain]  Cd Length: 62  Bit Score: 39.50  E-value: 5.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   714 TKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPR----DNEIVtIRGPSRGVNKAHEELK 772
Cdd:cd22407    1 TERLDIPKVYHPFIAGPNNENVKELQEETGVRINIPPpsvnKDEIV-VSGEKEGVAQAVAKIK 62
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 865-929 5.65e-04

fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourth one.


Pssm-ID: 411836 [Multi-domain]  Cd Length: 62  Bit Score: 39.08  E-value: 5.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   865 VLKIDHKYHKSIVGSGGHILREIISKAGGeeirnkSVDIPNADSENKDITVQGPQKFVKKVVEEI 929
Cdd:cd22408    3 SVEVPKSQHRFVIGPRGSTIQEILEETGC------SVEVPPNDSDSETITLRGPADKLGAALTLV 61
KH-I_Vigilin_rpt3 cd22407
third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 1168-1212 5.95e-04

third type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the third one.


Pssm-ID: 411835 [Multi-domain]  Cd Length: 62  Bit Score: 39.11  E-value: 5.95e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 1173344  1168 IVGPGGSNIKKIREAADVIINVPRKSDKVNDVVyIRGTKAGVEKA 1212
Cdd:cd22407   14 IAGPNNENVKELQEETGVRINIPPPSVNKDEIV-VSGEKEGVAQA 57
KH-I_PCBP3_rpt3 cd22522
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ...
 629-704 6.94e-04

third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) and similar proteins; PCBP3, also called alpha-CP3, or PCBP3-overlapping transcript, or PCBP3-overlapping transcript 1, or heterogeneous nuclear ribonucleoprotein E3, or hnRNP E3, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It can function as a repressor dependent on binding to single-strand and double-stranded poly(C) sequences. PCBP3 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411950 [Multi-domain]  Cd Length: 75  Bit Score: 39.33  E-value: 6.94e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173344   629 NSPSSKSKMTvnIPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASKdktvEVTLTGLEYNLTHAKKYLAA 704
Cdd:cd22522    5 SPPASTHELT--IPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGSSER----QITITGSPANISLAQYLINA 74
KH-I_AKAP1 cd22395
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ...
 786-847 7.59e-04

type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa, or AKAP 149, or dual specificity A-kinase-anchoring protein 1, or D-AKAP-1, or protein kinase A-anchoring protein 1 (PRKA1), or spermatid A-kinase anchor protein 84, or S-AKAP84, is a novel developmentally regulated A kinase anchor protein of male germ cells. It binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.


Pssm-ID: 411823 [Multi-domain]  Cd Length: 68  Bit Score: 39.04  E-value: 7.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173344   786 VINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKSTDPKAQetgevELEITGSRQNIKDA 847
Cdd:cd22395    3 EFEVPSELVGRLIGKQGRNVKQLKQKSGAKIYIKPHPYTQNFQ-----ICSIEGTQQQIDKA 59
KH-I_Mextli_like cd22454
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ...
 937-1006 7.91e-04

type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic translation initiation factor 4E-binding protein Mextli and similar proteins; Mextli is a novel eukaryotic translation initiation factor 4E-binding protein that promotes translation in Drosophila melanogaster.


Pssm-ID: 411882 [Multi-domain]  Cd Length: 71  Bit Score: 39.22  E-value: 7.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173344   937 ENSVTKTIDIPAERKGALIGPGG--IVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAeKKILNEII 1006
Cdd:cd22454    1 TGQTTIEVVIPNADVGKVIGKGGetIKRIEALTDTVITFERVNGGSPNREVQITGSPDNVAAA-KRLIEDTI 71
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 639-692 1.00e-03

seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the seventh one.


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 38.84  E-value: 1.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1173344   639 VNIPANSVARLIGNKGSNLQQIREKFACQIDIPneENNNASKDKTVEVTLTGLE 692
Cdd:cd22452    6 IKVSPRYFGRIIGPGGSNINQIREKSGCFINVP--KKNKESDVITLRGTKEGVE 57
KH-I_Vigilin_rpt6 cd02394
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 638-700 1.02e-03

sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one.


Pssm-ID: 411804 [Multi-domain]  Cd Length: 68  Bit Score: 38.71  E-value: 1.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   638 TVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEEnnnaskDKTVEVTLTGLEYNLTHAKK 700
Cdd:cd02394    5 TIEIDPKFHGHIIGKGGANIKRIREESGVSIRIPDDE------ANSDEIRIEGSPEGVKKAKA 61
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
 785-858 1.02e-03

type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.


Pssm-ID: 411803 [Multi-domain]  Cd Length: 70  Bit Score: 38.61  E-value: 1.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173344   785 MVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFlqkstdpkaQETGEVELEITgSRQNIKDAAKRVESIVAEA 858
Cdd:cd02393    6 TTIKIPPDKIGDVIGPGGKTIRAIIEETGAKIDI---------EDDGTVTIFAT-DKESAEAAKAMIEDIVAEP 69
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
 787-855 1.09e-03

first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the first one.


Pssm-ID: 411856 [Multi-domain]  Cd Length: 74  Bit Score: 38.85  E-value: 1.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   787 INVPAEHVPRIIGKNGDNINDIRAEYGVEMDFlqKSTDPkAQETGEVELEITGSRQNIKDAAKRVESIV 855
Cdd:cd22428    9 MKVPREAVGLIIGRQGATIKQIQKETGARIDF--KDEGS-GGELPERVLLIQGNPVQAQRAEEAIHQII 74
KH-I_ANKRD17 cd22502
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ...
 787-857 1.26e-03

type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 (ANKRD17) and similar proteins; ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


Pssm-ID: 411930 [Multi-domain]  Cd Length: 71  Bit Score: 38.58  E-value: 1.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173344   787 INVPAEHVPRIIGKNGDNINDIRAEYGVEMDFlqkstDPKAQETGEVELEITGSRQNIKDAAKRVESIVAE 857
Cdd:cd22502    5 VSVPSTVISRVIGRGGCNINAIREFTGAHIDI-----DKQKDKTGDRIITIRGGTESTRQATQLINALIKD 70
KH-I_IGF2BP_rpt4 cd22403
fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
 641-687 1.30e-03

fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/CRD-BP/VICKZ1, IGF2BP2/IMP-2/VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the fourth one.


Pssm-ID: 411831 [Multi-domain]  Cd Length: 66  Bit Score: 38.38  E-value: 1.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 1173344   641 IPANSVARLIGNKGSNLQQIREKFACQIDIPNEENNNASKDKTVEVT 687
Cdd:cd22403    6 VPSSMVGRIIGKGGQNVRELQRLTGAIIKLPRDQTPDEGDEVPVEII 52
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 864-930 1.32e-03

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 38.43  E-value: 1.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   864 EVLKIDHKYHKSIVGSGGHILREIiskaggEEIRNKSVDIPNADSENKD--ITVQGPQKFVKKVVEEIN 930
Cdd:cd00105    1 EEIEVPSELVGLIIGKGGSTIKEI------EEETGARIQIPKEGEGSGErvVTITGTPEAVEKAKELIE 63
KH-I_PNPT1 cd09033
type I K homology (KH) RNA-binding domain found in mitochondrial polyribonucleotide ...
 940-979 1.42e-03

type I K homology (KH) RNA-binding domain found in mitochondrial polyribonucleotide nucleotidyltransferase 1 (PNPT1) and similar proteins; PNPT1, also called 3'-5' RNA exonuclease OLD35, or PNPase old-35, or polynucleotide phosphorylase 1, or PNPase 1, or polynucleotide phosphorylase-like protein, is an RNA-binding protein implicated in numerous RNA metabolic processes. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. It acts as a mitochondrial intermembrane factor with RNA-processing exoribonulease activity. PNPT1 is a component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. It is involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules and required for correct processing and polyadenylation of mitochondrial mRNAs. PNPT1 also plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix.


Pssm-ID: 411809 [Multi-domain]  Cd Length: 67  Bit Score: 38.33  E-value: 1.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 1173344   940 VTKTIDIPAERKGALIGPGGIVRRQLESEF----------NINLFVPNKD 979
Cdd:cd09033    6 VTETLEVPPSKRAKFVGPGGYNIKKLQAETgvtitqvdeeTFSVFAPNQS 55
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 941-1003 1.49e-03

third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411876  Cd Length: 81  Bit Score: 38.66  E-value: 1.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173344   941 TKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSG-----------KITITGAPENVEKAEKKILN 1003
Cdd:cd22448    4 TLILKIPVQFHGSLIGQQGKYVNRLQEKYGVKINFPRENSSSNdtetkkpqapdEVTIRGGKKGVAEAKQELLE 77
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 714-777 1.52e-03

fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 38.40  E-value: 1.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173344   714 TKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDNEIV--TIRGPSRGVNKAHEELKALLDF 777
Cdd:cd22449    5 TVKFDVPAKYVPHIIGKKGANINKLREEYGVKIDFEDKTGEGnvEIKGSKKNVEEAKKRILSQIDE 70
KH-I_Rnc1_rpt3 cd22457
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
 942-997 1.57e-03

third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding protein Rnc1 and similar proteins; Rnc1, also called RNA-binding protein that suppresses calcineurin deletion 1, is an RNA-binding protein that acts as an important regulator of the posttranscriptional expression of the MAPK phosphatase Pmp1 in fission yeast. It binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression of Rnc1 suppresses the Cl(-) sensitivity of calcineurin deletion. The nuclear export of Rnc1 requires mRNA-binding ability and the mRNA export factor Rae1. Rnc1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411885 [Multi-domain]  Cd Length: 64  Bit Score: 38.21  E-value: 1.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344   942 KTIDIPAERKGALIGPGGI----VRRQLESEFNINLfVPNKDDPSGKITITGAPENVEKA 997
Cdd:cd22457    1 QNISIPPDMVGCIIGKGGSkiqeIRRLSGCKISIAK-APHDETGERMFTITGTPEANDRA 59
KH-I_Vigilin_rpt13 cd22416
thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 177-255 1.59e-03

thirteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the thirteenth one.


Pssm-ID: 411844 [Multi-domain]  Cd Length: 78  Bit Score: 38.37  E-value: 1.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   177 PINAVIEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEvnensydEDMDDTtsnVSLFGDFESVNLAKAKILAIVKE 255
Cdd:cd22416    1 PVTEEVNVPFDLHRFIIGQKGADVRKMMDEFDVNISIPPA-------ELQSDI---IKITGPPANVERAKAALLERVKE 69
KH-I_IGF2BP_rpt4 cd22403
fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ...
 784-839 1.79e-03

fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/CRD-BP/VICKZ1, IGF2BP2/IMP-2/VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the fourth one.


Pssm-ID: 411831 [Multi-domain]  Cd Length: 66  Bit Score: 37.99  E-value: 1.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1173344   784 KMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQkstDPKAQETGEVELEITG 839
Cdd:cd22403    1 RTEIRVPSSMVGRIIGKGGQNVRELQRLTGAIIKLPR---DQTPDEGDEVPVEIIG 53
KH-I_ScSCP160_rpt5 cd22450
fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 937-1001 1.89e-03

fifth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fifth one.


Pssm-ID: 411878  Cd Length: 80  Bit Score: 38.41  E-value: 1.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173344   937 ENSVTKTIDIPAERKGALIGPGGIVRRQL---------ESEFNINLFVPNKDDPSGKITITGAPENVEKAEKKI 1001
Cdd:cd22450    1 EDEVTRTIKVDRKYHRTIIGPGGSTLRELiskaggptdRQEQARLVRFPNQNSESDEVVIRGPKKIVEKIIAEI 74
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
 943-1008 1.96e-03

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 42.34  E-value: 1.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344    943 TIDIPAERKGALIGPGGIVRRQLESEFN--INLfvpnkdDPSGKITITGA-PENVEKAEKKIlNEIIRE 1008
Cdd:PRK11824  557 TIKIPPDKIRDVIGPGGKTIREITEETGakIDI------EDDGTVKIAATdGEAAEAAKERI-EGITAE 618
KH-I_MASK cd22404
type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family ...
 639-670 1.96e-03

type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family includes Drosophila melanogaster ankyrin repeat and KH domain-containing protein Mask, and its mammalian homologues Mask1/ANKHD1 and Mask2/ANKRD17. Mask, also called multiple ankyrin repeat single KH domain-containing protein, is a large ankyrin repeat and KH domain-containing protein involved in Drosophila receptor tyrosine kinase signaling. It acts as a mediator of receptor tyrosine kinase (RTK) signaling and may act either downstream of MAPK or transduce signaling through a parallel branch of the RTK pathway. Mask is required for the development and organization of indirect flight muscle sarcomeres by regulating the formation of M line and H zone and the correct assembly of thick and thin filaments in the sarcomere. Mask1/ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. Mask2/ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses.


Pssm-ID: 411832 [Multi-domain]  Cd Length: 71  Bit Score: 37.96  E-value: 1.96e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 1173344   639 VNIPANSVARLIGNKGSNLQQIREKFACQIDI 670
Cdd:cd22404    5 VTVPNSAISRVIGRGGCNINAIREVSGAHIEI 36
KH_I_FMR1_FXR_rpt3 cd22427
third type I K homology (KH) RNA-binding domain found in a family of fragile X mental ...
 787-847 2.08e-03

third type I K homology (KH) RNA-binding domain found in a family of fragile X mental retardation protein (FMR1) and fragile X related (FXR) proteins; The FMR1/FXR family includes FMR1 (also known as FMRP) and its two homologues, fragile X related 1 (FXR1) and 2 (FXR2). They are involved in translational regulation, particularly in neuronal cells and play an important role in the regulation of glutamate-mediated neuronal activity and plasticity. Each of these three proteins can form heteromers with the others, and each can also form homomers. Lack of expression of FMR1 results in mental retardation and macroorchidism. FXR1 and FXR2 may play important roles in the function of FMR1 and in the pathogenesis of the Fragile X Mental Retardation Syndrome. Members of this family contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411855 [Multi-domain]  Cd Length: 79  Bit Score: 38.36  E-value: 2.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   787 INVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKS--TDPKAQETGEVELEITGSRQNIKDA 847
Cdd:cd22427    6 FQVPRDLVGKVIGKNGRVIQEIVDKSGVVRVKIEGDneDGPRPREEGLVPFIFVGTREAIANA 68
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 502-606 2.15e-03

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 42.27  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344    502 ESSVAFVQFGDYYPNDNSILLVA---LTEDEDFKPSI-EEIQASLNKANESLNSLRTKQNNM-----ETKTYEFSEEVQD 572
Cdd:PRK15460  188 ETAQAYVASGEYYWNSGMFLFRAgryLEELKKYRPDIlDACEKAMSAVDPDLDFIRVDEEAFlacpeESVDYAVMERTAD 267

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1173344    573 SLFKPSSATWklimEDISEQEGHLQIKLHTPEEN 606
Cdd:PRK15460  268 AVVVPMDAGW----SDVGSWSSLWEISAHTAEGN 297
KH-I_PCBP_rpt1 cd22438
first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
 1168-1220 2.40e-03

first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411866 [Multi-domain]  Cd Length: 67  Bit Score: 37.62  E-value: 2.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1173344  1168 IVGPGGSNIKKIREAADVIINVPRKSDKvNDVVYIRGTKAGVEKAGEMVLKSL 1220
Cdd:cd22438   13 IIGKKGETIKKFREESGARINISDGSCP-ERIVTVTGTTDAVFKAFELICRKL 64
KH-I_ScSCP160_rpt3 cd22448
third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 1168-1220 2.48e-03

third type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411876  Cd Length: 81  Bit Score: 37.89  E-value: 2.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344  1168 IVGPGGSNIKKIREAADVIINVPRKSDKVN----------DVVYIRGTKAGVEKAGEMVLKSL 1220
Cdd:cd22448   17 LIGQQGKYVNRLQEKYGVKINFPRENSSSNdtetkkpqapDEVTIRGGKKGVAEAKQELLELL 79
KH-I_FUBP3_rpt2 cd22483
second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ...
 938-1008 3.01e-03

second type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411911 [Multi-domain]  Cd Length: 83  Bit Score: 37.96  E-value: 3.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   938 NSVTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDD-PSGK---ITITGAPENVEKAEKKILnEIIRE 1008
Cdd:cd22483    3 NSTIQEILIPASKVGLVIGKGGETIKQLQERTGVKMIMIQDGPlPTGAdkpLRITGDPFKVQQAREMVL-EIIRE 76
KH-I_Rnc1_rpt3 cd22457
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ...
 787-852 3.06e-03

third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding protein Rnc1 and similar proteins; Rnc1, also called RNA-binding protein that suppresses calcineurin deletion 1, is an RNA-binding protein that acts as an important regulator of the posttranscriptional expression of the MAPK phosphatase Pmp1 in fission yeast. It binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression of Rnc1 suppresses the Cl(-) sensitivity of calcineurin deletion. The nuclear export of Rnc1 requires mRNA-binding ability and the mRNA export factor Rae1. Rnc1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411885 [Multi-domain]  Cd Length: 64  Bit Score: 37.44  E-value: 3.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173344   787 INVPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKSTDpkaqETGEVELEITGSRQNIKDAAKRVE 852
Cdd:cd22457    3 ISIPPDMVGCIIGKGGSKIQEIRRLSGCKISIAKAPHD----ETGERMFTITGTPEANDRALRLLY 64
KH-I_ScSCP160_rpt7 cd22452
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 866-931 3.08e-03

seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the seventh one.


Pssm-ID: 411880 [Multi-domain]  Cd Length: 65  Bit Score: 37.30  E-value: 3.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   866 LKIDHKYHKSIVGSGGhilrEIISKaggeeIRNKS---VDIPNADSENKDITVQGPQKFVKKVVEEINK 931
Cdd:cd22452    6 IKVSPRYFGRIIGPGG----SNINQ-----IREKSgcfINVPKKNKESDVITLRGTKEGVEKAEEMIKK 65
KH-I_FUBP_rpt1 cd22396
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ...
 940-1006 3.18e-03

first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411824 [Multi-domain]  Cd Length: 68  Bit Score: 37.23  E-value: 3.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   940 VTKTIDIPAERKGALIGPGG--IVRRQLESEFNINLFVPNKDDPSGKITITGAPENVEKAeKKILNEII 1006
Cdd:cd22396    1 VTEEYKVPDKMVGLIIGRGGeqINRLQAESGAKIQIAPDSGGLPERPCTLTGTPDAIETA-KRLIDQIV 68
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 170-402 3.27e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.96  E-value: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344     170 LVKKLTKPINAvievpSKCKASIIGS-GGRTIRE-ISDAYEVKINV-SKEVNENSYDEDMDDTTSNVSLfgDFESVNLAK 246
Cdd:TIGR01612 1391 LIKKIKDDINL-----EECKSKIESTlDDKDIDEcIKKIKELKNHIlSEESNIDTYFKNADENNENVLL--LFKNIEMAD 1463

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344     247 AKILAIVKEETKNATIKLVVEDEKYLPYIDVSEFASDEGD------EEVKVQFYKKSGDIVILGPREKAKATKTSIQDyl 320
Cdd:TIGR01612 1464 NKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADknakaiEKNKELFEQYKKDVTELLNKYSALAIKNKFAK-- 1541

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173344     321 KKLASNLDEEKVKiPSKFQFLIDAEELKEKYNVIVTFPSTPDDElvsfVGLRDKVGEAITYARSSSKSYVVESLDISKAH 400
Cdd:TIGR01612 1542 TKKDSEIIIKEIK-DAHKKFILEAEKSEQKIKEIKKEKFRIEDD----AAKNDKSNKAAIDIQLSLENFENKFLKISDIK 1616


                   ..
gi 1173344     401 SK 402
Cdd:TIGR01612 1617 KK 1618
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 862-932 3.70e-03

sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the sixth one.


Pssm-ID: 411879 [Multi-domain]  Cd Length: 69  Bit Score: 37.05  E-value: 3.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173344   862 VTEVLKIDHKYHKSIVGSGGHILREIISKAGGeeirnkSVDIPNADSENKDITVQGPQKFVKKVVEEINKI 932
Cdd:cd22451    1 ASIDIDIPKEYHRAIIGKGGAVLRELEAETGC------RIQVPKKDDPSGKIRITGARDGVEAATAKILNI 65
KH-I_ScSCP160_rpt4 cd22449
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 937-1005 3.88e-03

fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fourth one.


Pssm-ID: 411877 [Multi-domain]  Cd Length: 70  Bit Score: 37.25  E-value: 3.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   937 ENSVTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDpSGKITITGAPENVEKAEKKILNEI 1005
Cdd:cd22449    1 ENGYTVKFDVPAKYVPHIIGKKGANINKLREEYGVKIDFEDKTG-EGNVEIKGSKKNVEEAKKRILSQI 68
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 781-852 3.89e-03

tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the tenth one.


Pssm-ID: 411841 [Multi-domain]  Cd Length: 66  Bit Score: 36.85  E-value: 3.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173344   781 NGHKMVINVPAEHVPRIIGKNGDNINDIRAEYGVEMDFlqkstdPKAQETGEVELEITGSRQNIKDAAKRVE 852
Cdd:cd22413    1 NSFTVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIF------PTARDEDQELITIIGTKEAVEKAKEELE 66
KH-I_Vigilin_rpt5 cd22409
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 712-776 4.63e-03

fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fifth one.


Pssm-ID: 411837 [Multi-domain]  Cd Length: 70  Bit Score: 36.79  E-value: 4.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173344   712 IITKELIVPVKFHGSLIGPHG-TYRNRLQEKYNVFINFPRDNEIVTIRGPSRGVNKAHEELKALLD 776
Cdd:cd22409    1 VVVAEVSAPSWLHRFIIGKKGaNIKKITQDLPKVHIEFTEGEDKIELEGPPEEVEVVREQLEAIVK 66
KH-I_ScSCP160_rpt1 cd22446
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 713-774 5.11e-03

first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the first one.


Pssm-ID: 411874 [Multi-domain]  Cd Length: 86  Bit Score: 37.39  E-value: 5.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   713 ITKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDNE-------------IVTIRGPSRGVNKAHEELKAL 774
Cdd:cd22446    7 VTITISVPSSVRGAIIGSRGKNLKSIQDKTGTKIQIPKRNEegnydeddddetvEISIEGDAEGVELAKKEIEAI 81
KH-I_PCBP_rpt2 cd02396
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
 789-857 5.21e-03

second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411806 [Multi-domain]  Cd Length: 72  Bit Score: 36.86  E-value: 5.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   789 VPAEHVPRIIGKNGDNINDIR----AEYGVEMDFLQKSTdpkaqetgEVELEITGSRQNIKDAAKRVESIVAE 857
Cdd:cd02396    8 VPASQCGSLIGKGGSKIKEIRestgASVQVASEMLPNST--------ERAVTISGSPEAITKCVEQICCVMLE 72
KH-I_PCBP_rpt3 cd22439
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ...
 941-998 5.72e-03

third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one.


Pssm-ID: 411867 [Multi-domain]  Cd Length: 68  Bit Score: 36.44  E-value: 5.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173344   941 TKTIDIPAERKGALIGPGG-----IvrRQLeSEFNINLFVPNKDDPSGKITITGAPENVEKAE 998
Cdd:cd22439    3 TQEITIPNDLIGCIIGKGGtkineI--RQL-SGATIKIANSEDGSTERSVTITGTPEAVSLAQ 62
KH-I_Vigilin_rpt2 cd22406
second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 638-699 6.14e-03

second type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the second one.


Pssm-ID: 411834 [Multi-domain]  Cd Length: 75  Bit Score: 36.90  E-value: 6.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173344   638 TVNIPANSVARLIGNKGSNLQQIREKFACQIDIPNEEnnnaskDKTVEVTLTGLEYNLTHAK 699
Cdd:cd22406    8 TVNIPKEHHRFILGKKGKKLQELELKTATKIVIPRQE------DNSDEIKITGTKEGIEKAR 63
KH-I_PEPPER_rpt2_like cd22460
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ...
 789-856 6.53e-03

second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH2 domain of PEPPER and FLK, as well as KH2 and KH4 domains of RCF3 and HEN4.


Pssm-ID: 411888 [Multi-domain]  Cd Length: 73  Bit Score: 36.44  E-value: 6.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344   789 VPAEHVPRIIGKNGDNINDIRAEYGVEMDFLQKSTDPKAQETGEVELEITGSRQNIKDAakrVESIVA 856
Cdd:cd22460    6 VASSQAGSLIGKGGAIIKQIREESGASVRILPEEELPPCASPDDRVVQISGEAQAVKKA---LELVSS 70
KH-I_MEX3_rpt2 cd22424
second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding ...
 940-1005 6.55e-03

second type I K homology (KH) RNA-binding domain found in the family of MEX-3 RNA-binding proteins; The MEX-3 protein family includes four members, MEX3A/RKHD4, MEX3B/RKHD3/RNF195, MEX3C/ RKHD2/RNF194, and MEX3D/RKHD1/RNF193/TINO. They are homologous of Caenorhabditis elegans MEX-3 protein, a translational regulator that specifies the posterior blastomere identity in the early embryo and contributes to the maintenance of the germline totipotency. Mex-3 proteins are RNA-binding phosphoproteins involved in post-transcriptional regulatory mechanisms. They are characterized by containing two K-homology (KH) RNA-binding domains and a C-terminal RING finger. They bind RNA through their KH domains and shuttle between the nucleus and the cytoplasm via the CRM1-dependent export pathway. The model corresponds to the second KH domain.


Pssm-ID: 411852 [Multi-domain]  Cd Length: 72  Bit Score: 36.55  E-value: 6.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344   940 VTKTIDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKD-DPSgkITITGAPENVEKAEKKILNEI 1005
Cdd:cd22424    4 TTIQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDkEPV--FEVTGMPENVERAREEIEAHI 68
KH-I_Vigilin_rpt15 cd22418
fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 1161-1218 6.70e-03

fifteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fifteenth one.


Pssm-ID: 411846 [Multi-domain]  Cd Length: 69  Bit Score: 36.48  E-value: 6.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1173344  1161 DTRRFNMIVGPGGSNIKKIREAADVIINVPRKSDKVNDVVYIRGTKAGVEKAGEMVLK 1218
Cdd:cd22418    8 DSRVHPRLIGARGKAIRKIMEDFKVDIRFPRSGDADPNLVTITGLEENVEECKDHLLN 65
KH-I_Vigilin_rpt10 cd22413
tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ...
 714-771 6.82e-03

tenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the tenth one.


Pssm-ID: 411841 [Multi-domain]  Cd Length: 66  Bit Score: 36.47  E-value: 6.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173344   714 TKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFP----RDNEIVTIRGPSRGVNKAHEEL 771
Cdd:cd22413    4 TVEIRAKPEYHRFLIGRGGANIRKIRDNTGARIIFPtardEDQELITIIGTKEAVEKAKEEL 65
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 787-852 7.21e-03

eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the eighth one.


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 36.03  E-value: 7.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173344   787 INVPAEHVPRIIGKNGDNINDIRAEYGVEMDFlqkstdPKAQETGEVeLEITGSRQNIKDAAKRVE 852
Cdd:cd22411    4 VPIFKQFHKNIIGKGGATIKKIREETNTRIDL------PEENSDSDV-ITITGKKEDVEKARERIL 62
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 714-769 7.28e-03

eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the eighth one.


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 36.03  E-value: 7.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   714 TKELIVPVKFHGSLIGPHGTYRNRLQEKYNVFINFPRDN---EIVTIRGPSRGVNKAHE 769
Cdd:cd22411    1 SIKVPIFKQFHKNIIGKGGATIKKIREETNTRIDLPEENsdsDVITITGKKEDVEKARE 59
KH-I_ScSCP160_rpt6 cd22451
sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ...
 182-256 8.21e-03

sixth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the sixth one.


Pssm-ID: 411879 [Multi-domain]  Cd Length: 69  Bit Score: 36.28  E-value: 8.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173344   182 IEVPSKCKASIIGSGGRTIREISDAYEVKINVSKEvnensydedmDDTTSNVSLFGDFESVNLAKAKILAIVKEE 256
Cdd:cd22451    5 IDIPKEYHRAIIGKGGAVLRELEAETGCRIQVPKK----------DDPSGKIRITGARDGVEAATAKILNISDEE 69
KH-I_Vigilin_rpt8 cd22411
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 182-250 9.13e-03

eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the eighth one.


Pssm-ID: 411839 [Multi-domain]  Cd Length: 62  Bit Score: 36.03  E-value: 9.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173344   182 IEVPSKCKASIIGSGGRTIREISDAYEVKINVSkevNENSYDEdmddttsNVSLFGDFESVNLAKAKIL 250
Cdd:cd22411    4 VPIFKQFHKNIIGKGGATIKKIREETNTRIDLP---EENSDSD-------VITITGKKEDVEKARERIL 62
KH-I_TDRKH_rpt1 cd22428
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ...
 944-1006 9.17e-03

first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the first one.


Pssm-ID: 411856 [Multi-domain]  Cd Length: 74  Bit Score: 36.16  E-value: 9.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173344   944 IDIPAERKGALIGPGGIVRRQLESEFNINLFVPNKDDPSGK----ITITGAPENVEKAEKKIlNEII 1006
Cdd:cd22428    9 MKVPREAVGLIIGRQGATIKQIQKETGARIDFKDEGSGGELpervLLIQGNPVQAQRAEEAI-HQII 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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